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Abstract:

Trypanosoma cruzi, the aetiological agent of Chagas' disease, is exposed to extremely different environment conditions during its life cycle, and transporters are key molecules for its adaptive regulation. Amino acids, and particularly arginine, are essential components in T. cruzi metabolism. In this work, a novel T. cruzi arginine permease was identified by screening different members of the AAAP family (amino acid/auxin permeases) in yeast complementation assays using a toxic arginine analogue. One gene candidate, TcAAAP411, was characterized as a very specific, high-affinity, l-arginine permease. This work is the first identification of the molecular components involved specifically in amino acid transport in T. cruzi and provides new insights for further validation of the TcAAAP family as functional permeases. © 2010 Federation of European Microbiological Societies.

Registro:

Documento: Artículo
Título:Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts
Autor:Carrillo, C.; Canepa, G.E.; Giacometti, A.; Bouvier, L.A.; Miranda, M.R.; De Los Milagros Camara, M.; Pereira, C.A.
Filiación:Fundación Instituto Leloir, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires and CONICET, Buenos Aires, Argentina
Departamento de Sustancias Vasoactivas, Instituto de Investigaciones Médicas Alfredo Lanari, Universidad de Buenos Aires and CONICET, Buenos Aires, Argentina
Palabras clave:AAAP family; Amino acid transport; Arginine permease; Chagas' disease; Trypanosoma cruzi; arginine; arginine permease; auxin permease; bacterial enzyme; canavanine; unclassified drug; active transport; amino acid transport; amino terminal sequence; article; bacterial strain; binding affinity; carboxy terminal sequence; controlled study; expression vector; gene identification; genetic analysis; nonhuman; parasite identification; parasite migration; priority journal; sensitivity and specificity; transport kinetics; Trypanosoma cruzi; yeast; Amino Acid Transport Systems, Basic; Arginine; Genetic Complementation Test; Protozoan Proteins; Recombinant Proteins; Saccharomyces cerevisiae; Trypanosoma cruzi; Trypanosoma cruzi
Año:2010
Volumen:306
Número:2
Página de inicio:97
Página de fin:102
DOI: http://dx.doi.org/10.1111/j.1574-6968.2010.01936.x
Título revista:FEMS Microbiology Letters
Título revista abreviado:FEMS Microbiol. Lett.
ISSN:03781097
CODEN:FMLED
CAS:arginine, 1119-34-2, 15595-35-4, 7004-12-8, 74-79-3; canavanine, 543-38-4; Amino Acid Transport Systems, Basic; Arginine, 74-79-3; Protozoan Proteins; Recombinant Proteins; arginine permease, 56626-25-6
PDF:https://bibliotecadigital.exactas.uba.ar/download/paper/paper_03781097_v306_n2_p97_Carrillo.pdf
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781097_v306_n2_p97_Carrillo

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Citas:

---------- APA ----------
Carrillo, C., Canepa, G.E., Giacometti, A., Bouvier, L.A., Miranda, M.R., De Los Milagros Camara, M. & Pereira, C.A. (2010) . Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts. FEMS Microbiology Letters, 306(2), 97-102.
http://dx.doi.org/10.1111/j.1574-6968.2010.01936.x
---------- CHICAGO ----------
Carrillo, C., Canepa, G.E., Giacometti, A., Bouvier, L.A., Miranda, M.R., De Los Milagros Camara, M., et al. "Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts" . FEMS Microbiology Letters 306, no. 2 (2010) : 97-102.
http://dx.doi.org/10.1111/j.1574-6968.2010.01936.x
---------- MLA ----------
Carrillo, C., Canepa, G.E., Giacometti, A., Bouvier, L.A., Miranda, M.R., De Los Milagros Camara, M., et al. "Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts" . FEMS Microbiology Letters, vol. 306, no. 2, 2010, pp. 97-102.
http://dx.doi.org/10.1111/j.1574-6968.2010.01936.x
---------- VANCOUVER ----------
Carrillo, C., Canepa, G.E., Giacometti, A., Bouvier, L.A., Miranda, M.R., De Los Milagros Camara, M., et al. Trypanosoma cruzi amino acid transporter TcAAAP411 mediates arginine uptake in yeasts. FEMS Microbiol. Lett. 2010;306(2):97-102.
http://dx.doi.org/10.1111/j.1574-6968.2010.01936.x